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P24815 (3BHS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
Alternative name(s):
3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I
Short name=3-beta-HSD I

Including the following 2 domains:

  1. 3-beta-hydroxy-Delta(5)-steroid dehydrogenase
    EC=1.1.1.145
    Alternative name(s):
    3-beta-hydroxy-5-ene steroid dehydrogenase
    Progesterone reductase
  2. Steroid Delta-isomerase
    EC=5.3.3.1
    Alternative name(s):
    Delta-5-3-ketosteroid isomerase
Gene names
Name:Hsd3b1
Synonyms:Hsd3b
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids.

Catalytic activity

A 3-beta-hydroxy-Delta(5)-steroid + NAD+ = a 3-oxo-Delta(5)-steroid + NADH.

A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid.

Pathway

Lipid metabolism; steroid biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.

Tissue specificity

Steroidogenic tissues (includes testes, ovaries and adrenal glands).

Sequence similarities

Belongs to the 3-beta-HSD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 3733723 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
PRO_0000087780

Regions

Transmembrane288 – 30821Helical; Potential

Sites

Active site1551Proton acceptor By similarity
Binding site1591NAD By similarity

Experimental info

Sequence conflict1281V → A in AAH52659. Ref.2
Sequence conflict3191L → S in AAH52659. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P24815 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 395F9D786C7BA010

FASTA37342,062
        10         20         30         40         50         60 
MAGWSCLVTG AGGFVGQRII KMLVQEKELQ EVRALDKVFR PETKEEFSKL QTKTKVTVLE 

        70         80         90        100        110        120 
GDILDAQCLR RACQGISVVI HTAAVIDVTG VIPRQTILDV NLKGTQNLLE ACVQASVPAF 

       130        140        150        160        170        180 
IFCSSVDVAG PNSYKKIVLN GHEEQNHEST WSDPYPYSKK MAEKAVLAAN GSMLKNGGTL 

       190        200        210        220        230        240 
NTCALRPMYI YGERSPFIFN AIIRALKNKG ILCVTGKFSI ANPVYVENVA WAHILAARGL 

       250        260        270        280        290        300 
RDPKKSTSIQ GQFYYISDDT PHQSYDDLNY TLSKEWGLRP NASWSLPLPL LYWLAFLLET 

       310        320        330        340        350        360 
VSFLLRPVYR YRPLFNRHLI TLSNSTFTFS YKKAQRDLGY EPLVNWEEAK QKTSEWIGTI 

       370 
VEQHREILDT KCQ

« Hide

References

« Hide 'large scale' references
[1]"Multiple forms of mouse 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase and differential expression in gonads, adrenal glands, liver, and kidneys of both sexes."
Bain P.A., Yoo M., Clarke T., Hammond S.H., Payne A.H.
Proc. Natl. Acad. Sci. U.S.A. 88:8870-8874(1991) [PubMed: 1924345] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: CD-1.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Egg.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M58567 mRNA. Translation: AAA37860.1.
BC052659 mRNA. Translation: AAH52659.1.
IPIIPI00229070.
PIRI49762.
RefSeqNP_032319.1. NM_008293.3.
UniGeneMm.140811.

3D structure databases

ProteinModelPortalP24815.
SMRP24815. Positions 4-360.
ModBaseSearch...

Protein-protein interaction databases

STRINGP24815.

Proteomic databases

PRIDEP24815.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000107016; ENSMUSP00000102630; ENSMUSG00000027871.
GeneID15492.
KEGGmmu:15492.

Organism-specific databases

CTD3283.
MGIMGI:96233. Hsd3b1.

Phylogenomic databases

eggNOGroNOG12122.
HOVERGENHBG000014.
InParanoidP24815.
OMAMAGWSCL.
PhylomeDBP24815.

Gene expression databases

ArrayExpressP24815.
BgeeP24815.
GenevestigatorP24815.
GermOnlineENSMUSG00000027871. Mus musculus.

Family and domain databases

InterProIPR002225. 3Beta_OHSteriod_DH/Estase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00070.
PfamPF01073. 3Beta_HSD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio288366.
SOURCESearch...

Entry information

Entry name3BHS1_MOUSE
AccessionPrimary (citable) accession number: P24815
Secondary accession number(s): Q7TQ00
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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